PMID: 2104983Jan 1, 1990Paper

GTP-binding Ypt1 protein and Ca2+ function independently in a cell-free protein transport reaction

Proceedings of the National Academy of Sciences of the United States of America
D BakerN Segev

Abstract

The 21-kDa GTP-binding Ypt1 protein (Ypt1p) is required for protein transport from the endoplasmic reticulum to the Golgi complex in yeast extracts. Ypt1 antibodies block transport; this inhibition is alleviated by competition with excess purified Ypt1p produced in bacteria. Furthermore, extracts of cells carrying the mutation ypt1-1 are defective in transport, but transport is restored if a cytosolic fraction from wild-type cells is provided. The in vitro transport reaction also requires physiological levels of Ca2+. However, Ypt1p functions independently of Ca2+. First, buffering the free Ca2+ at concentrations ranging from 1 nM to 10 microM does not relieve inhibition by Ypt1 antibodies. Second, consumption of a Ca2+-requiring intermediate that accumulates in Ca2+-deficient incubations is not inhibited by anti-Ypt1 antibodies, although completion of transport requires ATP and an N-ethylmaleimide-sensitive factor. Thus, Ypt1p and Ca2+ are required at distinct steps.

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Citations

Oct 1, 1990·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·A P Newman, S Ferro-Novick
Oct 1, 1992·Plant Molecular Biology·S Y Bednarek, N V Raikhel
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Aug 1, 1992·Proceedings of the National Academy of Sciences of the United States of America·K Römisch, R Schekman
Jan 15, 1992·Proceedings of the National Academy of Sciences of the United States of America·K PalmeJ Schell
Feb 15, 1992·Proceedings of the National Academy of Sciences of the United States of America·D J JinC A Gross
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Sep 15, 1994·Annals of the New York Academy of Sciences·B GoudV Slepnev
Mar 9, 1994·Annals of the New York Academy of Sciences·B GoudV Mayau

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